کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
443397 692718 2013 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Toward an understanding of the sequence and structural basis of allosteric proteins
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
Toward an understanding of the sequence and structural basis of allosteric proteins
چکیده انگلیسی

Allostery is the most efficient means of regulating protein functions, ranging from the control of metabolic mechanisms to signal transduction pathways. Although allosteric regulation has been recognized for half a century, our knowledge is limited to the characteristics of allosteric proteins and the structural coupling of allosteric sites and modulators. In this paper, we present a comprehensive analysis of allosteric proteins that provides insight into the foundation of allosteric interactions by revealing a series of common features in the allosteric proteins. Allosteric proteins mainly appear in transferases, and phosphorylation is the most common type of modification found in allosteric proteins. Disorders related to allosteric proteins primarily comprise metabolic diseases and cancers. In general, allosteric proteins prefer to exist as monomers or even-numbered multimers. Greater stability and hydrophobicity are observed in allosteric proteins than in general proteins. Further analysis of the allosteric sites reveals a series of buried and compact pockets composed of significantly greater hydrophobic surface area than the corresponding orthosteric sites. The hydrophobicity of the allosteric sites plays a dominant role in the binding of allosteric modulators as observed in the analysis of 106 diverse allosteric protein–modulator pairs. These results may be of great significance in predicting which proteins are allosteric and in designing novel triggers to inhibit or activate proteins of interest.

Figure optionsDownload high-quality image (192 K)Download as PowerPoint slideHighlight
► We analyzed the sequence and structural characteristics of allosteric proteins.
► Allosteric proteins prefer to exist as monomers or even-numbered multimers.
► Greater stability and hydrophobicity are observed in allosteric proteins than in general proteins.
► Hydrophobicity of allosteric sites plays a dominant role in the binding of allosteric modulators.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Graphics and Modelling - Volume 40, March 2013, Pages 30–39
نویسندگان
, , , , , , , ,